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Database: UniProt/TrEMBL
Entry: G8PRV7_PSEUV
LinkDB: G8PRV7_PSEUV
Original site: G8PRV7_PSEUV 
ID   G8PRV7_PSEUV            Unreviewed;       456 AA.
AC   G8PRV7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   26-NOV-2014, entry version 14.
DE   SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:AEV37313.1};
DE            EC=3.2.1.22 {ECO:0000313|EMBL:AEV37313.1};
GN   Name=melA {ECO:0000313|EMBL:AEV37313.1};
GN   OrderedLocusNames=PSE_2805 {ECO:0000313|EMBL:AEV37313.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV37313.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and
RT   symbiotically interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Note=Binds 1 NAD per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|RuleBase:RU361152}.
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DR   EMBL; CP003147; AEV37313.1; -; Genomic_DNA.
DR   RefSeq; WP_014285395.1; NC_016642.1.
DR   RefSeq; YP_005081335.1; NC_016642.1.
DR   EnsemblBacteria; AEV37313; AEV37313; PSE_2805.
DR   GeneID; 11590693; -.
DR   KEGG; psf:PSE_2805; -.
DR   KO; K07406; -.
DR   OMA; HDLDIPY; -.
DR   BioCyc; PSP911045:GJTQ-2833-MONOMER; -.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005634};
KW   Glycosidase {ECO:0000256|RuleBase:RU361152,
KW   ECO:0000313|EMBL:AEV37313.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361152,
KW   ECO:0000313|EMBL:AEV37313.1}; NAD {ECO:0000256|RuleBase:RU361152};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005634}.
SQ   SEQUENCE   456 AA;  51794 MW;  C82CB81816F31C62 CRC64;
     MARNPKITFV GAGSTTFMKN IIGDILQRPA LSGAHVALMD INEERLGESE IVARKLIATL
     GVSATVSTHT NQMEALDSAD FVVVAFQIGG YEPCTVTDFE IPKKYDLRQT IADTLGIGGI
     MRGLRTVPHL WSICEDMLKV CPEAVMLQYV NPMAINTWAI AQKYPQIKQV GLCHSVQGTV
     KELAHDLDLD PANIRYRCAG INHMAFYLYL EEIKEDGTFE DLYPRLMEGY REGRYPKPST
     WNPRCQNVVR YEMLTRLGHF VTESSEHFSE YVPWFIKRDR PDLLEKFSIP LDEYPVRCVE
     QIERWKSQVE DYKNAESIEV ERSQEYASTI MNSIWTGEPS VIYGNVQNKG YITSLPQDCA
     VEVPCLVDRN GIQPTHISKL PAQLAALMRT NIGPQELTVE ALMTENREHI YHAAMLDPHT
     AAELDLEQIW AMVDELLEAH KDWLPAWTQK QVLETA
//
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